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RHOV_BOVIN
ID   RHOV_BOVIN              Reviewed;         236 AA.
AC   Q17QI8;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Rho-related GTP-binding protein RhoV;
GN   Name=Rhov {ECO:0000250|UniProtKB:Q7L0Q8};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1] {ECO:0000312|EMBL:AAI18336.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford {ECO:0000312|EMBL:AAI18336.1};
RC   TISSUE=Fetal skin {ECO:0000312|EMBL:AAI18336.1};
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays a role in the control of the actin cytoskeleton via
CC       activation of the JNK pathway. {ECO:0000250|UniProtKB:Q9Z1Y0}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q7L0Q8};
CC   -!- SUBUNIT: Interacts with PAK2. {ECO:0000250|UniProtKB:Q9Z1Y0}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P61586,
CC       ECO:0000250|UniProtKB:Q9Z1Y0}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:P61586, ECO:0000250|UniProtKB:Q9Z1Y0};
CC       Cytoplasmic side {ECO:0000250|UniProtKB:P61586,
CC       ECO:0000250|UniProtKB:Q9Z1Y0}. Endosome membrane
CC       {ECO:0000250|UniProtKB:P61586, ECO:0000250|UniProtKB:Q9Z1Y0}; Lipid-
CC       anchor {ECO:0000250|UniProtKB:P61586, ECO:0000250|UniProtKB:Q9Z1Y0};
CC       Cytoplasmic side {ECO:0000250|UniProtKB:P61586,
CC       ECO:0000250|UniProtKB:Q9Z1Y0}. Note=Treatment with TNF activates
CC       endosomal but not plasma membrane RHOV. {ECO:0000250|UniProtKB:P61586,
CC       ECO:0000250|UniProtKB:Q9Z1Y0}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC       {ECO:0000250|UniProtKB:Q9Z1Y0}.
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DR   EMBL; BC118335; AAI18336.1; -; mRNA.
DR   RefSeq; NP_001069567.1; NM_001076099.1.
DR   AlphaFoldDB; Q17QI8; -.
DR   SMR; Q17QI8; -.
DR   STRING; 9913.ENSBTAP00000021672; -.
DR   PaxDb; Q17QI8; -.
DR   PRIDE; Q17QI8; -.
DR   Ensembl; ENSBTAT00000083826; ENSBTAP00000066710; ENSBTAG00000053721.
DR   GeneID; 538143; -.
DR   KEGG; bta:538143; -.
DR   CTD; 171177; -.
DR   VEuPathDB; HostDB:ENSBTAG00000053721; -.
DR   VGNC; VGNC:55140; RHOV.
DR   eggNOG; KOG0393; Eukaryota.
DR   GeneTree; ENSGT00940000157624; -.
DR   HOGENOM; CLU_041217_21_5_1; -.
DR   InParanoid; Q17QI8; -.
DR   OMA; TPELGIK; -.
DR   OrthoDB; 1091615at2759; -.
DR   Proteomes; UP000009136; Chromosome 10.
DR   Bgee; ENSBTAG00000053721; Expressed in surface of tongue and 81 other tissues.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0032488; P:Cdc42 protein signal transduction; IBA:GO_Central.
DR   GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR   GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   InterPro; IPR003578; Small_GTPase_Rho.
DR   PANTHER; PTHR24072; PTHR24072; 1.
DR   Pfam; PF00071; Ras; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51420; RHO; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Endosome; GTP-binding; Lipoprotein; Magnesium; Membrane;
KW   Metal-binding; Nucleotide-binding; Palmitate; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..236
FT                   /note="Rho-related GTP-binding protein RhoV"
FT                   /id="PRO_0000326437"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         38..45
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z1Y0"
FT   BINDING         85..89
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q7L0Q8"
FT   BINDING         143..146
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P61586"
FT   MOD_RES         25
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96L33"
FT   LIPID           234
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z1Y0"
SQ   SEQUENCE   236 AA;  25971 MW;  3E30E35DCC0856A5 CRC64;
     MPPRELSEAE SSPLRSPTPP PGRGSASPEL GIKCVLVGDG AVGKSSLIVS YTCNGYPARY
     RPTALDTFSV QVLVDGAPVR IELWDTAGQE DLDRLRSLCY PDTDVFLACF SVVQPSSFQN
     ITEKWLPEIR THNPQAPVLL VGTQADLRDD VNVLIQLDQG GREGPVPQPQ AQGLAEKIRA
     CCYLECSALT QKNLKEVFDS AILSAIEHKA RLEKKLNAKG VRTLSRCRWK KFFCFV
 
 
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